Fhod1 Reference Search Result - Rat Genome Database

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RGD ID	Title	Citation	Abstract	PubMed	Pub Date
11086311	FHOD1 interaction with nesprin-2G mediates TAN line formation and nuclear movement.	Kutscheidt S, etal., Nat Cell Biol. 2014 Jul;16(7):708-15. doi: 10.1038/ncb2981. Epub 2014 Jun 1.	Active positioning of the nucleus is integral to division, migration and differentiation of mammalian cells. Fibroblasts polarizing for migration orient their centrosomes by actin-dependent nuclear movement. This nuclear movement depends on nesprin-2 giant (N2G), a large, actin-binding outer nuclear ... (more) membrane component of transmembrane actin-associated (TAN) lines that couple nuclei to moving actin cables. Here, we identify the diaphanous formin FHOD1 as an interaction partner of N2G. Silencing FHOD1 expression or expression of fragments containing binding sites for N2G or FHOD1 disrupted nuclear movement and centrosome orientation in polarizing fibroblasts. Unexpectedly, silencing of FHOD1 expression did not affect the formation or rearward flow of dorsal actin cables required for nuclear positioning. Rather, N2G-FHOD1 interaction provided a second connection to actin cables essential for TAN line formation and thus nuclear movement. These results reveal a unique function for a formin in coupling an organelle to actin filaments for translocation, and suggest that TAN lines require multi-point attachments to actin cables to resist the large forces necessary to move the nucleus.	24880667	2014-06-01
11574235	The formins FHOD1 and INF2 regulate inter- and intra-structural contractility of podosomes.	Panzer L, etal., J Cell Sci. 2016 Jan 15;129(2):298-313. doi: 10.1242/jcs.177691. Epub 2015 Nov 30.	Podosomes are actin-rich adhesion structures that depend on Arp2/3-complex-based actin nucleation. We now report the identification of the formins FHOD1 and INF2 as novel components and additional actin-based regulators of podosomes in primary human macrophages. ... (more) FHOD1 surrounds the podosome core and is also present at podosome-connecting cables, whereas INF2 localizes at the podosome cap structure. Using a variety of microscopy-based methods; including a semiautomated podosome reformation assay, measurement of podosome oscillations, FRAP analysis of single podosomes, and structured illumination microscopy, both formins were found to regulate different aspects of podosome-associated contractility, with FHOD1 mediating actomyosin contractility between podosomes, and INF2 regulating contractile events at individual podosomes. Moreover, INF2 was found to be a crucial regulator of podosome de novo formation and size. Collectively, we identify FHOD1 and INF2 as novel regulators of inter- and intra-structural contractility of podosomes. Podosomes thus present as one of the few currently identified structures which depend on the concerted activity of both Arp2/3 complex and specific formins and might serve as a model system for the analysis of complex actin architectures in cells.	26621033	2016-01-15